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  • View Data Sheet

    Description:

    Stromal Cell-Derived Factor-1 beta Rat Recombinant (CXCL12)

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    Product # :

    CHM-248

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    Description

    SDF-1 beta Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8.4 kDa. The Rat SDF-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rat SDF1B protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phsophate buffer pH-7.4 and 0.15M NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized SDF-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.

    • Background

      What is the molecular weight/Mw of CXCL12 RAT BETA Protein?
      CXCL12 RAT BETA Protein has a total Mw of 8.4kDa.

      What is the source or expression system of CXCL12 RAT BETA Protein?
      Escherichia Coli.

      What is the Purity of CXCL12 RAT BETA Protein?
      CXCL12 RAT BETA Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL12 RAT BETA Protein?
      The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.

      What is the amino acid sequence of CXCL12 RAT BETA Protein?
      KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.

      What applications can CXCL12 RAT BETA Protein be used in?
      CXCL12 RAT BETA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL12 RAT BETA Protein?
      The endotoxin level is minimal, CXCL12 RAT BETA Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL12 RAT BETA that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL12 RAT BETA?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Sdf 1B Rat
  • View Data Sheet

    Description:

    GM-CSF Receptor Alpha Sf9 Human Recombinant

    Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX,  GMCSFR, CD116, SMDP4, GMR.                  

    Product # :

    CYT-1044

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    Description

    CSF2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (20-320a.a.) and having a molecular mass of 35.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CSF2RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CSF2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

    More Info

    • Introduction

      GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.

    • Synonyms

      Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPLIPEKSD LRTVAPASSL NVRFDSRTMN LSWDCQENTT FSKCFLTDKK NRVVEPRLSN NECSCTFREI CLHEGVTFEV HVNTSQRGFQ QKLLYPNSGR EGTAAQNFSC FIYNADLMNC TWARGPTAPR DVQYFLYIRN SKRRREIRCP YYIQDSGTHV GCHLDNLSGL TSRNYFLVNG TSREIGIQFF DSLLDTKKIE RFNPPSNVTV RCNTTHCLVR WKQPRTYQKL SYLDFQYQLD VHRKNTQPGT ENLLINVSGD LENRYNFPSS EPRAKHSVKI RAADVRILNW SSWSEAIEFG SDDGHHHHHH

    • Background

      GM-CSF Receptor Alpha Human Recombinant: A Glimpse into Its Potential and Implications

      Abstract:

      Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) receptor alpha, a pivotal component in the GM-CSF signaling pathway, has been the focal point of numerous studies pertaining to hematopoiesis and immune responses. This paper provides an overview of the GM-CSF receptor alpha human recombinant, exploring its characteristics, production techniques, and potential therapeutic applications.

      Introduction

      GM-CSF, a cytokine responsible for the differentiation and proliferation of white blood cells, functions by binding to its receptor, GM-CSF receptor. The alpha subunit (GM-CSFRα) of this receptor plays a crucial role in ligand binding and is essential for initiating cellular responses. Modern biotechnological advancements have led to the successful production of its human recombinant form, offering new avenues in medical research.

      Recombinant GM-CSFRα:

      Production and Features Recombinant GM-CSFRα is synthesized using cutting-edge recombinant DNA technologies, predominantly in bacterial or mammalian expression systems. This human recombinant form retains its ability to bind to GM-CSF, maintaining its biological functionality and providing myriad research opportunities.

      Therapeutic and Clinical Prospects

      1. Autoimmune Diseases: GM-CSF is often overexpressed in various autoimmune disorders. By utilizing recombinant GM-CSFRα as a potential decoy receptor, it's feasible to mitigate the effects of excessive GM-CSF, offering a new therapeutic strategy.
      2. Hematopoietic Disorders: Given its integral role in white blood cell development, recombinant GM-CSFRα might hold promise in treatments or as a diagnostic tool for certain hematological conditions.
      3. Research Paradigm: Beyond therapeutic applications, the recombinant GM-CSFRα can serve as an invaluable research tool to elucidate the nuances of GM-CSF signaling, aiding in the understanding of immune response mechanisms.

      Conclusion:

      GM-CSF receptor alpha human recombinant stands at the forefront of exciting research and therapeutic potential. While its full capabilities are yet to be realized, current insights underscore its significance in the realms of immunology and medicine.

      What is the molecular weight/Mw of CD116 Protein?
      CD116 Protein has a total Mw of 35.9kDa.

      What is the source or expression system of CD116 Protein?
      Sf9, Baculovirus cells.
      What is the Purity of CD116 Protein?
      CD116 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD116 Protein?
      Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

      What is the amino acid sequence of CD116 Protein?
      CD116 Protein is composed from 310 amino acids.

      What applications can CD116 Protein be used in?
      CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD116 Protein?
      The endotoxin level is minimal, CD116 Protein was purified using conventional chromatography techniques

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gmcsf Receptor
  • View Data Sheet

    Description:

    Pregnancy Specific Beta-1-Glycoprotein 5 Human Recombinant, Sf9

    Pregnancy Specific Beta-1-Glycoprotein 5, Pregnancy-Specific Beta-1 Glycoprotein, Fetal Liver Non-Specific Cross-Reactive Antigen 3, Pregnancy-Specific Beta-1-Glycoprotein 5, FL-NCA-3, PS-beta-G-5, PSBG-5, PSG.

    Product # :

    PRO-2459

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    Description

    PSG5 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 310 amino acids (35-335 a.a.) and having a molecular mass of 35.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PSG5 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PSG5 protein solution (0.25mg/ml) contains 20mM Tris (pH6.8), 40% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PSG5 belongs to the PSG family, which are a highly connected group of secreted glycoproteins, vastly expressed in fetal placental syncytiotrophoblast cells. PSGs are can be found in serum from the first 2-3 weeks of pregnancy and at higher levels as the pregnancy progresses, up to e point where they are the highest fetal protein found in maternal blood at term. PSG5’s role is inducing secretion of TH2-type cytokines from monocytes and modulating the maternal immune system throughout the pregnancy, thus defending the semi-allotypic fetus from rejection.

    • Synonyms

      Pregnancy Specific Beta-1-Glycoprotein 5, Pregnancy-Specific Beta-1 Glycoprotein, Fetal Liver Non-Specific Cross-Reactive Antigen 3, Pregnancy-Specific Beta-1-Glycoprotein 5, FL-NCA-3, PS-beta-G-5, PSBG-5, PSG.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADLQVTIEAL PPKVSEGKDV LLLVHNLPQN LAGYIWYKGQ LMDLYHYITS YVVDGQINIY GPAYTGRETV YSNASLLIQN VTREDAGSYT LHIIKRGDRT RGVTGYFTFN LYLKLPKPYI TINNSKPREN KDVLAFTCEP KSENYTYIWW LNGQSLPVSP RVKRPIENRI LILPSVTRNE
      TGPYECEIRD RDGGMRSDPV TLNVLYGPDL PSIYPSFTYY RSGENLYLSC FAESNPPAEY FWTINGKFQQ SGQKLSIPQI TTKHRGLYTC SVRNSATGKE SSKSMTVEVS APSGIGRLPL LNPIHHHHHH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Psg5 Protein
  • View Data Sheet

    Description:

    B-cell Activating Factor Human Recombinant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-307

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    Description

    BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 17.7kDa.

      What is the source or expression system of BLYS Protein?
      Escherichia Coli.

      What is the Purity of BLYS Protein?
      BLYS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BLYS Protein?
      The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

      What is the amino acid sequence of BLYS Protein?
      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

      What applications can BLYS Protein be used in?
      BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BLYS Protein?
      The endotoxin level is minimal, BLYS Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Blys Human
  • View Data Sheet

    Description:

    Insulin-Like Growth Factor Binding Protein-4 Human

    Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4, BP-4, HT29-IGFBP.

    Product # :

    CYT-030

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    Description

    IGFBP-4 Human Recombinant amino acids Asp22- Glu258, produced in HEK293 cells and fused with a polyhistidine tag at the C-terminus. IGFBP4 predicted Mw is 27kDa and on SDS-PAGE appears as a 32kDa band under denaturing conditions.IGFBP4 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    IGFBP 4 was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is 0.01-0.09µg/ml as measured by its ability to inhibit the biological activity of IGFII (20ng/ml) on MCF7 human breast adenocarcinoma cells.

    More Info

    • Introduction

      Insulin-like growth factor-binding protein 4 (IGFBP-4) belongs to the insulin-like growth factor binding protein (IGFBP) family. IGFBP4 includes an IGFBP domain and a thyroglobulin type-I domain. IGFBP4 binds both insulin-like growth factors (IGFs) I and II. IGFBP-4 circulates in the plasma in both glycosylated and non-glycosylated forms. IGFBPs can either inhibit or enhance the biological activities of IGF, or act in an IGF independent manner. IGFBP-4 is exceptional since it consistently inhibits several cancer cells in vivo and in vitro, suggesting that it may function as an apoptotic factor. IGFBP4 is produced by all colon cancer cells. Binding of IGFBP-4 prolongs the half-life of the IGFs and changes their interaction with cell surface receptors.

    • Synonyms

      Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4, BP-4, HT29-IGFBP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGFBP4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IGFBP4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE + His Tag.

    • Background

      What is the molecular weight/Mw of IGFBP4 HUMAN Protein?
      IGFBP4 HUMAN Protein has a total Mw of 27kDa.

      What is the source or expression system of IGFBP4 HUMAN Protein?
      HEK293 cells.

      What is the Purity of IGFBP4 HUMAN Protein?
      IGFBP4 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGFBP4 HUMAN Protein?
      The ED50 range is 0.01-0.09µg/ml as measured by its ability to inhibit the biological activity of IGFII (20ng/ml) on MCF7 human breast adenocarcinoma cells.
      What is the amino acid sequence of IGFBP4 HUMAN Protein?
      DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE + His Tag.

      What applications can IGFBP4 HUMAN Protein be used in?
      IGFBP4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGFBP4 HUMAN Protein?
      The endotoxin level is minimal, IGFBP4 HUMAN Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Igfbp 4 Human
  • View Data Sheet

    Description:

    Transforming Growth Factor-Beta 3 Human Recombinant, CHO

    Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

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    CYT-1259

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    Description

    TGFB3 Human Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

    Purity

    Greater than 97.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

    More Info

    • Synonyms

      Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TGFB3 in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

    • Background

      Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tgfb3 Human
  • View Data Sheet

    Description:

    Activin A Receptor Type II-Like 1 Human Recombinant

    Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.

    Product # :

    CYT-920

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    Description

    ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.

    • Background

      The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant

      1. Abstract

      This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.

      2. Introduction

      ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.

      3. Structure and Signaling of ACVRL1

      ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.

      4. Biological Functions of ACVRL1

      ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.

      5. ACVRL1 in Disease Pathology

      Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.

      6. Therapeutic Potential of ACVRL1

      Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.

      7. Conclusion and Future Perspectives

      Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen

      What is the molecular weight / Mw of ACVRL1 Protein?
      ACVRL1 Protein has a total Mw of 11.5kDa.

      What is the source or expression system of ACVRL1 Protein?
      Sf9, Insect cells.

      What is the Purity of ACVRL1 Protein?
      ACVRL1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ACVRL1 Protein?
      The biological functionality of ACVRL1 Protein will be determined in the future.

      What is the amino acid sequence of ACVRL1 Protein?
      DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.

      What applications can ACVRL1 Protein be used in?
      ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ACVRL1 Protein?
      The endotoxin level is minimal, ACVRL1 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Acvrl1 Human
  • View Data Sheet

    Description:

    Neurotrophin-1 Human Recombinant

    Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.

    Product # :

    CYT-869

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    Description

    Neurotrophin-1 Human Recombinant (28-225) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 199 amino acids and having a molecular mass of 22kDa.The NNT-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NNT-1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

    More Info

    • Introduction

      Cardiotrophin-like cytokine (CLC/ NNT-1) belongs to the IL-6 family of cytokines. All family members share the receptor subunit gp130, which belongs to the type I cytokine receptor superfamily. NNT1 is a trophic factor for motor neurons, a stimulator of ACTH release from corticotrophs, and an inducer of IgE synthesis and B cell proliferation. Cells expressing NNT-1 include embryonic muscle, lung epithelium, and mesenchyme. NNT1 binds to and activates the ILST/gp130 receptor.

    • Synonyms

      Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Neurotrophin-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NNT1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NNT1 in sterile 18M-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

    • Background

      What is the molecular weight/Mw of CLCF Protein?
      CLCF Protein has a total Mw of 22kDa.

      What is the source or expression system of CLCF Protein?
      Escherichia Coli.

      What is the Purity of CLCF Protein?
      CLCF Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CLCF Protein?
      The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

      What is the amino acid sequence of CLCF Protein?
      MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

      What applications can CLCF Protein be used in?
      CLCF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CLCF Protein?
      The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nnt1 Human
  • View Data Sheet

    Description:

    Transforming Growth Factor Beta 2 Human Recombinant

    Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    Product # :

    CYT-441

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    Description

    TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

    More Info

    • Introduction

      TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
      EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
      PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tgfb2 Human
  • View Data Sheet

    Description:

    Platelet-derived Growth Factor AA Human Recombinant, Yeast

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

    Product # :

    CYT-568

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    Description

    PDGF-AA Human Recombinant produced in Yeast is a homodimeric, glycosilated, polypeptide chain containing 2 x 110 amino acids and having a total molecular mass of 34 kDa. PDGF-AA is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    The protein was lyophilized with 20mM sodium phosphate buffer.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was found to be 1ng/ml  corresponding to a Specific Activity of 1,000,000IU/mg calculated by the ability to stimulate the proliferation of mouse 3T3 fibroblasts (PNAS 94, 10205, 1997. Biochemistry, 1996, 35, 12077).

    More Info

    • Introduction

      PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PDGF-AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized PDGF-AA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Pdgf Aa Human Yeast
  • View Data Sheet

    Description:

    NTF2-like Export Factor 2 Human Recombinant

    NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.

    Product # :

    PRO-1051

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    Description

    NXT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-197 a.a) and having a molecular mass of 25.3kDa.NXT2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NXT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nuclear transport factor 2-like export factor 2 (NXT2) belongs to the NXT family proteins which are commonly involved in exporting nuclear RNA in eukaryotic cells. The NXT2 protein is a regulator of protein export for NES-containing proteins. In addition, NXT2 associates with NXF1, NXF2, NXF3 and NXF5 and has a role in mRNA nuclear export. NXT2 has a critical role in upholding morphogenetic integrity of embryonic heart in vertebrate species. The NXT2 protein contains a nuclear transport factor 2 (NTF2) domain, which has a vital role in the trafficking of macromolecules, ions, and small molecules between the cytoplasm and nucleus, it may also have a role in mRNA nuclear export.

    • Synonyms

      NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMRKYRS HWSQGDREGY QRRSNYYEGP HTSHSSPADR TREEVVTPTL PEHTATRSQM ATSLDFKTYV DQACRAAEEF VNIYYETMDK RRRALTRLYL DKATLIWNGN AVSGLDALNN FFDTLPSSEF QVNMLDCQPV HEQATQSQTT VLVVTSGTVK
      FDGNKQHFFN QNFLLTAQST PNNTVWKIAS DCFRFQDWSS S.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nxt2 Human
  • View Data Sheet

    Description:

    Batroxobin

    Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    Product # :

    PRO-2146

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    Description

    Batroxobin, isolated from Bothrops atrox snake venom, has an Mw of approximately 43kDa.

    Formulation

    The Batroxobin protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    More Info

    • Introduction

      Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
      Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
      Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin.

    • Synonyms

      Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Store the lyophilized Batroxobin between 2-8°C. Do not freeze!

    • Solubility

      It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

    • Unit Definition

      100BU [Batroxobin Units]=1mg.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Batroxobin Native
  • View Data Sheet

    Description:

    Anti-Mullerian Hormone Human Recombinant, HEK

    Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF. 

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    PRO-2665

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    Description

    AMH Human Recombinant is a single, glycosylated polypeptide chain containing 439 amino acids (19-451a.a) and having a molecular mass of 46.5kDa (calculated). AMH is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293

    Formulation

    AMH filtered (0.4 µm) and lyophilized in PBS and 5% (w/v) trehalose.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.

    • Synonyms

      Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      LLGTEALRAE EPAVGTSGLI FREDLDWPPG SPQEPLCLVA LGGDSNGSSS PLRVVGALSA YEQAFLGAVQ RARWGPRDLA TFGVCNTGDR QAALPSLRRL GAWLRDPGGQ RLVVLHLEEV TWEPTPSLRF QEPPPGGAGP PELALLVLYP GPGPEVTVTR AGLPGAQSLC PSRDTRYLVL AVDRPAGAWR GSGLALTLQP RGEDSRLSTA RLQALLFGDD HRCFTRMTPA LLLLPRSEPA PLPAHGQLDT VPFPPPRPSA ELEESPPSAD PFLETLTRLV RALRVPPARA SAPRLALDPD ALAGFPQGLV NLSDPAALER LLDGEEPLLL LLRPTAATTG DPAPLHDPTS APWATALARR VAAELQAAAA ELRSLPGLPP ATAPLLARLL ALCPGGPGGL GDPLRALLLL KALQGLRVEW RGRDPRGPGR AQRHHHHHH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Anti Mullerian Hormone Human
  • View Data Sheet

    Description:

    Stromal Cell-Derived Factor-1 beta Human Recombinant (CXCL12), His Tag

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    Product # :

    CHM-249

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    Description

    SDF-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 93 amino acids (22-93 a.a.) and having a molecular mass of 10.8 KDa. The SDF-1b is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SDF-1 beta His Tag protein contains 20mM Tris-HCl buffer pH-8 and 10% glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor. The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM.

    • Background

      What is the molecular weight/Mw of CXCL12 HUMAN BETA, HIS Protein?
      CXCL12 HUMAN BETA, HIS Protein has a total Mw of 10.8kDa.

      What is the source or expression system of CXCL12 HUMAN BETA, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL12 HUMAN BETA, HIS Protein?
      CXCL12 HUMAN BETA, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL12 HUMAN BETA, HIS Protein?
      The biological functionality of CXCL12 HUMAN BETA, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL12 HUMAN BETA, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM.

      What applications can CXCL12 HUMAN BETA, HIS Protein be used in?
      CXCL12 HUMAN BETA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL12 HUMAN BETA, HIS Protein?
      The endotoxin level is minimal, CXCL12 HUMAN BETA, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL12 HUMAN BETA, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL12 HUMAN BETA, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Sdf 1B Human His
  • View Data Sheet

    Description:

    Epigen Human Recombinant, Sf9

    Epithelial mitogen,  EPG, Epithelial Mitogen Homolog (Mouse), Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.

    Product # :

    CYT-1038

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    • sds-page

    Description

    EPGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 97 amino acids (23-110a.a.) and having a molecular mass of 10.8kDa.EPGN is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    EPGN protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

    • Synonyms

      Epithelial mitogen, EPG, Epithelial Mitogen Homolog (Mouse), Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE KHHHHHH.

    • Background

      What is the molecular weight/Mw of EPIGEN Protein?
      EPIGEN Protein has a total Mw of 10.8kDa.

      What is the source or expression system of EPIGEN Protein?
      Sf9, Insect cells.

      What is the Purity of EPIGEN Protein?
      EPIGEN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of EPIGEN Protein?
      The biological functionality of EPIGEN Protein will be determined in the future.

      What is the amino acid sequence of EPIGEN Protein?
      ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE KHHHHHH.

      What applications can EPIGEN Protein be used in?
      EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EPIGEN Protein?
      The endotoxin level is minimal, EPIGEN Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Epgn
  • View Data Sheet

    Description:

    Tumor Necrosis Factor Receptor 13B Human Recombinant, His Tag

    CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

    Product # :

    CYT-032

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    Description

    TACI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids (1- 165a.a.) and having a molecular mass of 20.9kDa. The TACI is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TACI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.

    • Synonyms

      CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Taci Human
  • View Data Sheet

    Description:

    Jun Proto-Oncogene (1-241 a.a.) Human Recombinant

    Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

    Product # :

    PKA-001

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    Description

    C-JUN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.

    • Synonyms

      Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cjun Human
  • View Data Sheet

    Description:

    Melanoma Inhibitory Activity 2 Human Recombinant

    MIA-2, MIA2, Melanoma Inhibitory Activity 2, FLJ22404.

    Product # :

    CYT-638

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    Description

    MIA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain consisting of 101 amino having a total molecular mass of 11.5 kDa.The MIA2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MIA2 protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Phosphate buffer pH=7.4 and 150mM NaCl.

    Purity

    Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      MIA2 performs as a tumour suppressor in hepatocellular carcinoma. MIA2is a novel acute phase protein which its expression is found in the liver and reacts to liver damage in chronic liver diseases and is considerably higher in severe fibrosis patients . MIA2 is induced by IL6, TGF-B & and conditioned medium from activated hepatic stellate cells. MIA2 is is mainly expressed in hepatocytes.

    • Synonyms

      MIA-2, MIA2, Melanoma Inhibitory Activity 2, FLJ22404.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIA2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIA2 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized MIA2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLESTKLLAD LKKCGDLECE ALINRVSAMR DYRGPDCRYL NFTKGEEISV YVKLAGERED LWAGSKGKEF GYFPRDAVQI EEVFISEEIQ MSTKESDFLC L.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mia2 Human
  • View Data Sheet

    Description:

    Ectodysplasin A Receptor, Mouse Anti Human

    Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.

    Product # :

    ANT-560

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.

    • Synonyms

      Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human EDAR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EDAR protein 27-448 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT19E8AT.

    • Applications

      EDAR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      EDAR antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Edar Antibody
  • View Data Sheet

    Description:

    Macrophage Colony Stimulating Factor Mouse Recombinant, Sf9

    M-Csf, Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, C87615, MCSF, op, Processedmacrophage colony-stimulating factor 1.

    Product # :

    CYT-1141

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    Description

    MCSF Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids (33-187 aa) and having a molecular mass of 19.1 kDa.MCSF is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The MCSF solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cells. ED50 range for this effect is ≤ 4ng/ml.

    More Info

    • Introduction

      Macrophage Colony Stimulating Factor (M CSF) or colony stimulating factor 1, is a cytokine, that promoted differentiation in hematopoietic stem cells to macrophages. Another role of M CSF is to bind to its receptor (colony stimulating factor 1 receptor) and to take part in placenta growth and development.

    • Synonyms

      M-Csf, Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, C87615, MCSF, op, Processedmacrophage colony-stimulating factor 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPKEVSEHC SHMIGNGHLK VLQQLIDSQM ETSCQIAFEF VDQEQLDDPV CYLKKAFFLV
      QDIIDETMRF KDNTPNANAT ERLQELSNNL NSCFTKDYEE QNKACVRTFH ETPLQLLEKI
      KNFFNETKNL LEKDWNIFTK NCNNSFAKCS SRDVVTKPHH HHHH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mcsf Mouse
  • View Data Sheet

    Description:

    Growth and Differentiation factor 7 Human Recombinant

    Growth Differentiation Factor 7, GDF-7, Growth/Differentiation Factor 7, BMP12, GDF7.

    Product # :

    CYT-870

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    Description

    GDF7 Human Recombinant (322-450) produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 28kDa.The GDF-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in HCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as determined by inducing alkaline phosphatase production by mouse ATDC5 cells, is less than 1.25µg/ml.

    More Info

    • Introduction

      Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.

    • Synonyms

      Growth Differentiation Factor 7, GDF-7, Growth/Differentiation Factor 7, BMP12, GDF7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GDF-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TALAGTRTAQ GSGGGAGRGH GRRGRSRCSR KPLHVDFKEL GWDDWIIAPL DYEAYHCEGL CDFPLRSHLE PTNHAIIQTL LNSMAPDAAP ASCCVPARLS PISILYIDAA NNVVYKQYED MVVEACGCR.

    • Background

      What is the molecular weight/Mw of GDF7 Protein?
      GDF7 Protein has a total Mw of 28kDa.

      What is the source or expression system of GDF7 Protein?
      Escherichia Coli.

      What is the Purity of GDF7 Protein?
      GDF7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF7 Protein?
      The ED50, as determined by inducing alkaline phosphatase production by mouse ATDC5 cells, is less than 1.25µg/ml.

      What is the amino acid sequence of GDF7 Protein?
      TALAGTRTAQ GSGGGAGRGH GRRGRSRCSR KPLHVDFKEL GWDDWIIAPL DYEAYHCEGL CDFPLRSHLE PTNHAIIQTL LNSMAPDAAP ASCCVPARLS PISILYIDAA NNVVYKQYED MVVEACGCR.

      What applications can GDF7 Protein be used in?
      GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF7 Protein?
      The endotoxin level is minimal, GDF7 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gdf7 Human
  • View Data Sheet

    Description:

    Activin-B Human Recombinant, Active

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-057

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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

    More Info

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.

    • Background

      An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active

      1. Abstract

      Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.

      2. Introduction

      The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.

      3. Structure and Synthesis of Activin-B

      Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.

      4. Biological Functions of Activin-B

      Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.

      5. Activin-B in Regenerative Medicine

      Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.

      6. Activin-B and Reproductive Health

      Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.

      7. Activin-B in Cancer

      Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.

      8. Conclusion and Future Perspectives

      Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

      What is the Purity of Activin B Protein?
      Activin B Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of Activin B Protein?
      The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

      What is the endotoxin level for Activin B Protein?
      The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

      What applications can ACTIVIN B Protein be used in?
      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Activin B Human Active
  • View Data Sheet

    Description:

    Galectin-3 Human Recombinant

    Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.

    Product # :

    CYT-606

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    Description

    LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids and having a molecular mass of 26.2kDa. The LGALS3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-3 protein was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10 mM sodium phosphate and 50mM sodium chloride, pH 7.5.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.

    • Synonyms

      Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Galectin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized LGALS3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.

    • Background

      What is the molecular weight/Mw of LGALS3 HUMAN Protein?
      LGALS3 HUMAN Protein has a total Mw of 26.2kDa.

      What is the source or expression system of LGALS3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS3 HUMAN Protein?
      LGALS3 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS3 HUMAN Protein?
      The biological functionality of LGALS3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of LGALS3 HUMAN Protein?
      MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.

      What applications can LGALS3 HUMAN Protein be used in?
      LGALS3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS3 HUMAN Protein?
      The endotoxin level is minimal, LGALS3 HUMAN Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Galectin 3 Human
  • View Data Sheet

    Description:

    Thymic Stromal Lymphopoietin Receptor Human Recombinant

    CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.

    Product # :

    CYT-742

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TSLPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (23-231 a.a.) and having a molecular mass of 26.6kDa.TSLPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TSLPR protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.

    • Synonyms

      CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SK.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tslpr Human